Search results for: Mouse Anti-Human Amyloid P Antibodies
#23621497 2013/04/26 To Up
Monitoring systemic amyloidosis using MRI measurements of the extracellular volume fraction.
We report the in vivo evaluation, in a murine model, of MRI measurements of the extracellular volume fraction (ECV) for the detection and monitoring of systemic amyloidosis. A new inducible transgenic model was used, with increased production of mouse serum amyloid A protein controlled by oral administration of doxycycline, that causes both the usual hepatic and splenic amyloidosis and also cardiac deposits. ECV was measured in vivo by equilibrium contrast MRI in the heart and liver of 11 amyloidotic and 10 control mice. There was no difference in the cardiac function between groups, but ECV was significantly increased in the heart, mean (standard deviation) 0.20 (0.05) versus 0.14 (0.04), p < 0.005, and liver, 0.27 (0.04) versus 0.15 (0.04), p < 0.0005, of amyloidotic animals and was strongly correlated with the histological amyloid score, myocardium, ρ = 0.67, p < 0.01; liver, ρ = 0.87, p < 0.01. In a further four mice that received human serum amyloid P component (SAP) followed by anti-human SAP antibody, a treatment to eliminate visceral amyloid deposits, ECV in the liver and spleen returned to baseline after therapy (p < 0.01). MRI measurement of ECV is a sensitive marker of amyloid deposits with potential application for early detection and monitoring therapies promoting their clearance.Adrienne E Campbell-Washburn, Anthony N Price, Stephan Ellmerich, J Paul Simons, Raya Al-Shawi, Tammy L Kalber, Rupinder Ghatrora, Philip N Hawkins, James C Moon, Roger J Ordidge, Mark B Pepys, Mark F Lythgoe
2570 related Products with: Monitoring systemic amyloidosis using MRI measurements of the extracellular volume fraction.
0.1mg1mg500gm10mg50μl1mg100ug1.0ml 5 G1mg1.0mg100ugRelated Pathways
#10027926 // To Up
Impaired lysosomal processing of beta2-microglobulin by infiltrating macrophages in dialysis amyloidosis.
Macrophages may participate in amyloid fibril formation by processing the protein precursor. Although this theory seems to apply for amyloidosis, in which proteolytic cleavage is a prerequisite for amyloid fibril formation, it has not been demonstrated for beta2-microglobulin (beta2m) amyloidosis. We aimed to establish the role played by macrophages in beta2m amyloidosis.M García-García, Argilés, A Gouin-Charnet, M Durfort, J García-Valero, G Mourad
2189 related Products with: Impaired lysosomal processing of beta2-microglobulin by infiltrating macrophages in dialysis amyloidosis.
100 96 tests96 wells (1 kit)100 assays100 μgRelated Pathways
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